arising from: T. S. Slater et al. Nature Ecology & Evolution https://doi.org/10.1038/s41559-023-02177-8 (2023)

Slater et al.¹ analysed the chemical composition of untreated and experimentally degraded feathers from extant birds and fossils. The authors concluded that the dominant β-sheet structure of corneous β-proteins progressively undergoes alteration to α-helices with increasing temperature and suggested that (α-)keratins and α-helices in fossil feathers are probably artefacts of fossilization. However, we contend that the infrared data they presented could alternatively support the transformation of the β-sheet structure into disordered structures rather than α-helices. Moreover, we posit that their interpretation of the infrared data for fossil feathers from the Cretaceous overlooks the potential contributions of eumelanin residues.

arising from: T. S. Slater et al. Nature Ecology & Evolution https://doi.org/10.1038/s41559-023-02177-8 (2023)

斯莱特等人。 ¹分析了现存鸟类和化石中未经处理和实验降解的羽毛的化学成分。作者得出结论，随着温度的升高，角质 β 蛋白的主要 β 片层结构逐渐转变为 α 螺旋，并表明化石羽毛中的 (α-) 角蛋白和 α 螺旋可能是化石化的产物。然而，我们认为他们提供的红外数据可以支持β-折叠结构转变为无序结构而不是α-螺旋。此外，我们假设他们对白垩纪羽毛化石红外数据的解释忽略了真黑色素残留物的潜在贡献。